Evidence map›Paper›PMID 19720826›Full record

ArticleThe Journal of biological chemistry2009

Asymmetric signal transduction through paralogs that comprise a genetic switch for sugar sensing in Saccharomyces cerevisiae.

Jeffrey Sabina, Mark Johnston

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed, 1 pooled it
1.1field-weighted citation impact, top 25% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 1 synthesis or guideline pooled it, 30 citations in OpenAlex.

  1. Pooled it
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  9. Review
  10. The glucose signaling network in yeast.Biochimica et biophysica acta · 2013
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Jeffrey SabinaDepartment of Genetics, Washington University in Saint Louis, St. Louis, Missouri 63108, USA.
Mark Johnston
University of Colorado Denver · US

Funding

GLUCOSE SENSING AND SIGNALLING IN YEASTR01GM032540 · NIGMS · WASHINGTON UNIVERSITY · PI JOHNSTON, HENRY MARK · 1985 to 2017
$5.7M
Dissecting the wiring of yeast's glucose sensing circuitF32GM076967 · NIGMS · WASHINGTON UNIVERSITY · PI SABINA, JEFFREY · 2006 to 2008
$145k
NIGMS NIH HHS GM076967NIGMS NIH HHS GM32540NIGMS NIH HHS R01 GM032540
6 · The paper itself

Abstract

Efficient uptake of glucose is especially critical to Saccharomyces cerevisiae because its preference to ferment this carbon source demands high flux through glycolysis. Glucose induces expression of HXT genes encoding hexose transporters through a signal generated by the Snf3 and Rgt2 glucose sensors that leads to depletion of the transcriptional regulators Mth1 and Std1. These paralogous proteins bind to Rgt1 and enable it to repress expression of HXT genes. Here we show that Mth1 and Std1 can substitute for one another and provide nearly normal regulation of their targets. However, their roles in the glucose signal transduction cascade have diverged significantly. Mth1 is the prominent effector of Rgt1 function because it is the more abundant of the two paralogs under conditions in which both are active (in the absence of glucose). Moreover, the cellular level of Mth1 is quite sensitive to the amount of available glucose. The abundance of Std1 protein, on the other hand, remains essentially constant over a similar range of glucose concentrations. The signal generated by low levels of glucose is amplified by rapid depletion of Mth1; the velocity of this depletion is dependent on both its rate of degradation and swift repression of MTH1 transcription by the Snf1-Mig1 glucose repression pathway. Quantitation of the contributions of Mth1 and Std1 to regulation of HXT expression reveals the unique roles played by each paralog in integrating nutrient availability with metabolic capacity: Mth1 is the primary regulator; Std1 serves to buffer the response to glucose.

Indexed as

Adaptor Proteins, Signal TransducingDose-Response Relationship, DrugGene Expression Regulation, FungalGlucoseIntracellular Signaling Peptides and ProteinsMonosaccharide Transport ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSignal TransductionSweetening AgentsTranscription, GeneticAdaptor Proteins, Signal TransducingGlucoseIntracellular Signaling Peptides and ProteinsMonosaccharide Transport ProteinsMTH1 protein, S cerevisiaeRGT2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSNF3 protein, S cerevisiaeSTD1 protein, S cerevisiaeSweetening Agents

Identifiers

PMID19720826
PMCPMC2786032
OpenAlexW1964268317

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.